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Volumn 180, Issue 3, 1998, Pages 505-513

Immunolocalization of Hsp60 in Legionella pneumophila

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONIN; HEAT SHOCK PROTEIN 60; MONOCLONAL ANTIBODY; POLYCLONAL ANTIBODY;

EID: 0031910013     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.3.505-513.1998     Document Type: Article
Times cited : (97)

References (57)
  • 1
    • 0027417230 scopus 로고
    • Phenotypic modulation by Legionella pneumophila upon infection of macrophages
    • Abu Kwaik, Y., B. I. Eisenstein, and N. C. Engleberg. 1993. Phenotypic modulation by Legionella pneumophila upon infection of macrophages. Infect. Immun. 61:1320-1329.
    • (1993) Infect. Immun. , vol.61 , pp. 1320-1329
    • Abu Kwaik, Y.1    Eisenstein, B.I.2    Engleberg, N.C.3
  • 2
    • 0345612100 scopus 로고    scopus 로고
    • Transcriptional regulation of the macrophage-induced gene (gspA) of Legionella pneumophila and phenotypic characterization of a null mutant
    • Abu Kwaik, Y., L.-Y. Gao, O. S. Harb, and B. J. Stone. 1997. Transcriptional regulation of the macrophage-induced gene (gspA) of Legionella pneumophila and phenotypic characterization of a null mutant. Mol. Microbiol. 24:629-642.
    • (1997) Mol. Microbiol. , vol.24 , pp. 629-642
    • Abu Kwaik, Y.1    Gao, L.-Y.2    Harb, O.S.3    Stone, B.J.4
  • 3
    • 0031013397 scopus 로고    scopus 로고
    • The evolution and genetics of aphid endosymbionts
    • Baumann, P., N. A. Moran, and L. Baumann. 1997. The evolution and genetics of aphid endosymbionts. BioScience 47:12-20.
    • (1997) BioScience , vol.47 , pp. 12-20
    • Baumann, P.1    Moran, N.A.2    Baumann, L.3
  • 4
    • 0025093417 scopus 로고
    • An enhanced method for post-embedding immunocytochemical staining which preserves cell membranes
    • Berryman, M. A., and R. D. Rodewald. 1990. An enhanced method for post-embedding immunocytochemical staining which preserves cell membranes. J. Histochem. Cytochem. 38:159-170.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 159-170
    • Berryman, M.A.1    Rodewald, R.D.2
  • 5
    • 0027398036 scopus 로고
    • Major cytoplasmic membrane protein of Legionella pneumophila, a genus common antigen and member of the hsp 60 family of heat shock proteins, induces protective immunity in a guinea pig model of Legionnaires' disease
    • Blander, S. J., and M. A. Horwitz. 1993. Major cytoplasmic membrane protein of Legionella pneumophila, a genus common antigen and member of the hsp 60 family of heat shock proteins, induces protective immunity in a guinea pig model of Legionnaires' disease. J. Clin. Invest. 91:717-723.
    • (1993) J. Clin. Invest. , vol.91 , pp. 717-723
    • Blander, S.J.1    Horwitz, M.A.2
  • 6
    • 0025319891 scopus 로고
    • Characterization of a major 31-kilodalton peptidoglycan-bound protein of Legionella pneumophila
    • Butler, C. A., and P. S. Hoffman. 1990. Characterization of a major 31-kilodalton peptidoglycan-bound protein of Legionella pneumophila. J. Bacteriol. 172:2401-2407.
    • (1990) J. Bacteriol. , vol.172 , pp. 2401-2407
    • Butler, C.A.1    Hoffman, P.S.2
  • 7
    • 0021953774 scopus 로고
    • Disulfide-bonded outer membrane proteins in the genus Legionella
    • Butler, C. A., E. D. Street, T. P. Hatch, and P. S. Hoffman. 1985. Disulfide-bonded outer membrane proteins in the genus Legionella. Infect. Immun. 48:14-18.
    • (1985) Infect. Immun. , vol.48 , pp. 14-18
    • Butler, C.A.1    Street, E.D.2    Hatch, T.P.3    Hoffman, P.S.4
  • 8
    • 0022657708 scopus 로고
    • Serogroup specificity of Legionella pneumophila is related to lipopolysaccharide characteristics
    • Ciesielski, C. A., M. J. Blaser, and W.-L. L. Wang. 1986. Serogroup specificity of Legionella pneumophila is related to lipopolysaccharide characteristics. Infect. Immun. 51:397-404.
    • (1986) Infect. Immun. , vol.51 , pp. 397-404
    • Ciesielski, C.A.1    Blaser, M.J.2    Wang, W.-L.L.3
  • 9
    • 0027300506 scopus 로고
    • Heat-shock proteins: Molecular chaperones of protein biogenesis
    • Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat-shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402-414.
    • (1993) Microbiol. Rev. , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 11
    • 0026642506 scopus 로고
    • A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus
    • Ensgraber, M., and M. Loos. 1992. A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus. Infect. Immun. 60:3072-3078.
    • (1992) Infect. Immun. , vol.60 , pp. 3072-3078
    • Ensgraber, M.1    Loos, M.2
  • 12
    • 15644383285 scopus 로고    scopus 로고
    • Unpublished data
    • Faulkner, G. Unpublished data.
    • Faulkner, G.1
  • 13
    • 0029885305 scopus 로고
    • Elevated levels of Legionella pneumophila stress protein Hsp60 early in infection of human monocytes and L929 cells correlate with virulence
    • Fernandez, R. C., S. M. Logan, S. H. S. Lee, and P. S. Hoffman. 1946 Elevated levels of Legionella pneumophila stress protein Hsp60 early in infection of human monocytes and L929 cells correlate with virulence. Infect Immun. 64:1968-1976.
    • (1946) Infect Immun. , vol.64 , pp. 1968-1976
    • Fernandez, R.C.1    Logan, S.M.2    Lee, S.H.S.3    Hoffman, P.S.4
  • 14
    • 0030200018 scopus 로고    scopus 로고
    • The molecular ecology of legionellae
    • Fields, B. S. 1996. The molecular ecology of legionellae. Trends Microbiol. 4:286-290.
    • (1996) Trends Microbiol. , vol.4 , pp. 286-290
    • Fields, B.S.1
  • 15
    • 0000699069 scopus 로고
    • Molecular chaperone functions of hsp70 and hsp60 in protein folding
    • R. I. Morimoto, A. Tissières, and C. Georgopoulos (ed.), Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Frydman, J., and F.-U. Hartl. 1994. Molecular chaperone functions of hsp70 and hsp60 in protein folding, p. 251-283. In R. I. Morimoto, A. Tissières, and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 251-283
    • Frydman, J.1    Hartl, F.-U.2
  • 16
    • 0021964778 scopus 로고
    • Isolation and characterization of the cytoplasmic and outer membranes of the Legionnaires' disease bacterium Legionella pneumophila
    • Gabay, J. E., and M. A. Horwitz. 1985. Isolation and characterization of the cytoplasmic and outer membranes of the Legionnaires' disease bacterium Legionella pneumophila. J. Exp. Med. 161:409-422.
    • (1985) J. Exp. Med. , vol.161 , pp. 409-422
    • Gabay, J.E.1    Horwitz, M.A.2
  • 19
    • 0021887832 scopus 로고
    • Immunochemical characterization of a protein associated with Mycobacterium leprae cell wall
    • Gillis, T. P., R. A. Miller, D. B. Young, S. R. Khanolkar, and T. M. Buchanan. 1985. Immunochemical characterization of a protein associated with Mycobacterium leprae cell wall. Infect. Immun. 49:371-377.
    • (1985) Infect. Immun. , vol.49 , pp. 371-377
    • Gillis, T.P.1    Miller, R.A.2    Young, D.B.3    Khanolkar, S.R.4    Buchanan, T.M.5
  • 20
    • 0028960169 scopus 로고
    • Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells
    • Gupta, R. S. 1995. Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells. Mol. Microbiol. 15:1-11.
    • (1995) Mol. Microbiol. , vol.15 , pp. 1-11
    • Gupta, R.S.1
  • 22
  • 23
    • 0024314513 scopus 로고
    • Cloning and temperature-dependent expression in Escherichia coli of a Legionella pneumophila gene coding for a genus-common 60-kilodalton antigen
    • Hoffman, P. S., C. A. Butler, and F. D. Quinn. 1989. Cloning and temperature-dependent expression in Escherichia coli of a Legionella pneumophila gene coding for a genus-common 60-kilodalton antigen. Infect. Immun. 57:1731-1739.
    • (1989) Infect. Immun. , vol.57 , pp. 1731-1739
    • Hoffman, P.S.1    Butler, C.A.2    Quinn, F.D.3
  • 24
    • 0025113835 scopus 로고
    • Legionella pneumophila htpAB heat shock operon: Nucleotide sequence and expression of the 60-kilodalton antigen in L. pneumophila-infected HeLa cells
    • Hoffman, P. S., L. Houston, and C. A. Butler. 1990. Legionella pneumophila htpAB heat shock operon: nucleotide sequence and expression of the 60-kilodalton antigen in L. pneumophila-infected HeLa cells. Infect. Immun. 58:3380-3387.
    • (1990) Infect. Immun. , vol.58 , pp. 3380-3387
    • Hoffman, P.S.1    Houston, L.2    Butler, C.A.3
  • 25
    • 0029929131 scopus 로고    scopus 로고
    • Acidic pH changes receptor binding specificity of Helicobacter pylori: A binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization
    • Huesca, M., S. Borgia, P. Hoffman, and C. A. Lingwood. 1996. Acidic pH changes receptor binding specificity of Helicobacter pylori: a binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization. Infect. Immun. 64:2643-2648.
    • (1996) Infect. Immun. , vol.64 , pp. 2643-2648
    • Huesca, M.1    Borgia, S.2    Hoffman, P.3    Lingwood, C.A.4
  • 26
    • 0004909020 scopus 로고
    • Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120
    • Jäger, K. M., and B. Bergman. 1990. Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120. Planta 183:120-125.
    • (1990) Planta , vol.183 , pp. 120-125
    • Jäger, K.M.1    Bergman, B.2
  • 27
    • 0025953952 scopus 로고
    • Molecular chaperon produced by an intracellular symbiont
    • Kakeda, K., and H. Ishikawa. 1991. Molecular chaperon produced by an intracellular symbiont. J. Biochem. 110:583-587.
    • (1991) J. Biochem. , vol.110 , pp. 583-587
    • Kakeda, K.1    Ishikawa, H.2
  • 28
    • 0029798054 scopus 로고    scopus 로고
    • Interaction of the protein import and folding machineries in the chloroplast
    • Kessler, F., and G. Blobel. 1996. Interaction of the protein import and folding machineries in the chloroplast. Proc. Natl. Acad. Sci. USA 93:7684-7689.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7684-7689
    • Kessler, F.1    Blobel, G.2
  • 29
    • 0028008311 scopus 로고
    • Heat stress induces association of the GroEL analog chaperonin with thylakoid membranes in cyanobacterium, Synechocystis PCC 6803
    • Kovács, E., Z. Török, I. Horváth, and L. Vígh. 1994. Heat stress induces association of the GroEL analog chaperonin with thylakoid membranes in cyanobacterium, Synechocystis PCC 6803. Plant Physiol. Biochem. 32:285-293.
    • (1994) Plant Physiol. Biochem. , vol.32 , pp. 285-293
    • Kovács, E.1    Török, Z.2    Horváth, I.3    Vígh, L.4
  • 30
    • 0024287398 scopus 로고
    • Heat shock response of the chloroplast genome in Vigna sinensis
    • Krishnasamy, S., R. M. Mannan, M. Krishnan, and A. Gnanam. 1988. Heat shock response of the chloroplast genome in Vigna sinensis. J. Biol. Chem. 263:5104-5109.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5104-5109
    • Krishnasamy, S.1    Mannan, R.M.2    Krishnan, M.3    Gnanam, A.4
  • 31
    • 0029062216 scopus 로고
    • The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol
    • Kubota, H., G. Hynes, and K. Willison. 1995. The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. Eur. J. Biochem. 230:3-16.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 3-16
    • Kubota, H.1    Hynes, G.2    Willison, K.3
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 2642708641 scopus 로고
    • Localization of ribulose-bisphosphate carboxylase-oxygenase and its putative binding protein in the cell envelope of Chromatium vinosum
    • McFadden, B. A., J. A. Torres-Ruiz, and V. R. Franceschi. 1989. Localization of ribulose-bisphosphate carboxylase-oxygenase and its putative binding protein in the cell envelope of Chromatium vinosum. Planta 178:297-302.
    • (1989) Planta , vol.178 , pp. 297-302
    • McFadden, B.A.1    Torres-Ruiz, J.A.2    Franceschi, V.R.3
  • 35
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas, D., and S. Raina. 1997. Protein folding in the bacterial periplasm. J. Bacteriol. 179:2465-2471.
    • (1997) J. Bacteriol. , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 36
    • 0026596164 scopus 로고
    • Structures of chaperonins from an intracellular symbiont and their functional expression in Escherichia coli groE mutants
    • Ohtaka, C., H. Nakamura, and H. Ishikawa. 1992. Structures of chaperonins from an intracellular symbiont and their functional expression in Escherichia coli groE mutants. J. Bacteriol. 174:1869-1874.
    • (1992) J. Bacteriol. , vol.174 , pp. 1869-1874
    • Ohtaka, C.1    Nakamura, H.2    Ishikawa, H.3
  • 37
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell, D. A., and S. Lindquist. 1993. The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27:437-496.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 39
    • 0023858579 scopus 로고
    • Purification, partial characterization, and seroreactivity of a genuswide 60-kilodalton Legionella protein antigen
    • Pau, C.-P., B. B. Plikaytis, G. M. Carlone, and I. M. Warner. 1988. Purification, partial characterization, and seroreactivity of a genuswide 60-kilodalton Legionella protein antigen. J. Clin. Microbiol. 26:67-71.
    • (1988) J. Clin. Microbiol. , vol.26 , pp. 67-71
    • Pau, C.-P.1    Plikaytis, B.B.2    Carlone, G.M.3    Warner, I.M.4
  • 40
    • 0030021824 scopus 로고    scopus 로고
    • Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis
    • Phadnis, S. H., M. H. Parlow, M. Levy, D. Ilver, C. M. Caulkins, J. B. Connors, and B. E. Dunn. 1996. Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis. Infect. Immun. 64:905-912.
    • (1996) Infect. Immun. , vol.64 , pp. 905-912
    • Phadnis, S.H.1    Parlow, M.H.2    Levy, M.3    Ilver, D.4    Caulkins, C.M.5    Connors, J.B.6    Dunn, B.E.7
  • 41
    • 0023226335 scopus 로고
    • Purified 60-kilodalton Legionella protein antigen with Legionella-specific and nonspecific epitopes
    • Plikaytis, B. B., G. M. Carlone, C.-P. Pau, and H. W. Wilkinson. 1987. Purified 60-kilodalton Legionella protein antigen with Legionella-specific and nonspecific epitopes. J. Clin. Microbiol. 25:2080-2084.
    • (1987) J. Clin. Microbiol. , vol.25 , pp. 2080-2084
    • Plikaytis, B.B.1    Carlone, G.M.2    Pau, C.-P.3    Wilkinson, H.W.4
  • 42
    • 0028113172 scopus 로고
    • Bacterial heat-shock proteins induce cytokine mRNA and interleukin-1 secretion in macrophage cultures
    • Retzlaff, C., Y. Yamamoto, P. S. Hoffman, H. Friedman, and T. W. Klein. 1994. Bacterial heat-shock proteins induce cytokine mRNA and interleukin-1 secretion in macrophage cultures. Infect. Immun. 62:5689-5693.
    • (1994) Infect. Immun. , vol.62 , pp. 5689-5693
    • Retzlaff, C.1    Yamamoto, Y.2    Hoffman, P.S.3    Friedman, H.4    Klein, T.W.5
  • 43
    • 0029821214 scopus 로고    scopus 로고
    • Legionella pneumophila heat-shock protein-induced increase of interleukin-1β mRNA involves protein kinase C signaling in macrophages
    • Retzlaff, C., Y. Yamamoto, S. Okubo, P. S. Hoffman, H. Friedman, and T. W. Klein. 1996. Legionella pneumophila heat-shock protein-induced increase of interleukin-1β mRNA involves protein kinase C signaling in macrophages. Immunology 89:281-288.
    • (1996) Immunology , vol.89 , pp. 281-288
    • Retzlaff, C.1    Yamamoto, Y.2    Okubo, S.3    Hoffman, P.S.4    Friedman, H.5    Klein, T.W.6
  • 44
    • 0022658190 scopus 로고
    • Immunologic response of patients with legionellosis against major protein-containing antigens of Legionella pneumophila serogroup 1 as shown by immunoblot analysis
    • Sampson, J. S., B. B. Plikaytis, and H. W. Wilkinson. 1986. Immunologic response of patients with legionellosis against major protein-containing antigens of Legionella pneumophila serogroup 1 as shown by immunoblot analysis. J. Clin. Microbiol. 23:92-99.
    • (1986) J. Clin. Microbiol. , vol.23 , pp. 92-99
    • Sampson, J.S.1    Plikaytis, B.B.2    Wilkinson, H.W.3
  • 45
    • 0028116493 scopus 로고
    • Subcellular localization and chaperone activities of Borrelia burgdorferi Hsp60 and Hsp70
    • Scorpio, A., P. Johnson, A. Laquerre, and D. R. Nelson. 1994. Subcellular localization and chaperone activities of Borrelia burgdorferi Hsp60 and Hsp70. J. Bacteriol. 176:6449-6456.
    • (1994) J. Bacteriol. , vol.176 , pp. 6449-6456
    • Scorpio, A.1    Johnson, P.2    Laquerre, A.3    Nelson, D.R.4
  • 46
    • 0030023858 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells
    • Soltys, B. J., and R. S. Gupta. 1996. Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells. Exp. Cell Res. 222:16-27.
    • (1996) Exp. Cell Res. , vol.222 , pp. 16-27
    • Soltys, B.J.1    Gupta, R.S.2
  • 47
    • 0031147756 scopus 로고    scopus 로고
    • Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells
    • Soltys, B. J., and R. S. Gupta. 1997. Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells. Cell Biol. Int. 21:315-320.
    • (1997) Cell Biol. Int. , vol.21 , pp. 315-320
    • Soltys, B.J.1    Gupta, R.S.2
  • 48
    • 0026026915 scopus 로고
    • Genus-specific epitope on the 60-kilodalton Legionella heat shock protein recognized by a monoclonal antibody
    • Steinmetz, I., C. Rheinheimer, I. Hübner, and D. Bitter-Suermann. 1991. Genus-specific epitope on the 60-kilodalton Legionella heat shock protein recognized by a monoclonal antibody. J. Clin. Microbiol. 29:346-354.
    • (1991) J. Clin. Microbiol. , vol.29 , pp. 346-354
    • Steinmetz, I.1    Rheinheimer, C.2    Hübner, I.3    Bitter-Suermann, D.4
  • 49
    • 0029944643 scopus 로고    scopus 로고
    • De novo synthesis of Legionella pneumophila antigens during intracellular growth in phagocytic cells
    • Susa, M., J. Hacker, and R. Marre. 1996. De novo synthesis of Legionella pneumophila antigens during intracellular growth in phagocytic cells. Infect. Immun. 64:1679-1684.
    • (1996) Infect. Immun. , vol.64 , pp. 1679-1684
    • Susa, M.1    Hacker, J.2    Marre, R.3
  • 50
    • 0030903748 scopus 로고    scopus 로고
    • Evidence for a lipochaperonin: Association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions
    • Török, Z., I. Horváth, P. Goloubinoff, E. Kovács, A. Glatz, G. Balogh, and L. Vígh. 1997. Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions. Proc. Natl. Acad. Sci. USA 94:2192-2197.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2192-2197
    • Török, Z.1    Horváth, I.2    Goloubinoff, P.3    Kovács, E.4    Glatz, A.5    Balogh, G.6    Vígh, L.7
  • 51
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 53
    • 0027989755 scopus 로고
    • Endosymbiotic bacteria associated with circulative transmission of potato leafroll virus by Myzus persicae
    • van den Heuvel, J. F. J. M., M. Verbeek, and F. van der Wilk. 1994. Endosymbiotic bacteria associated with circulative transmission of potato leafroll virus by Myzus persicae. J. Gen. Virol. 75:2559-2565.
    • (1994) J. Gen. Virol. , vol.75 , pp. 2559-2565
    • Van Den Heuvel, J.F.J.M.1    Verbeek, M.2    Van Der Wilk, F.3
  • 54
    • 0023839992 scopus 로고
    • A heat shock operon in Coxiella burnetii produces a major antigen homologous to a protein in both mycobacteria and Escherichia coli
    • Vodkin, M. H., and J. C. Williams. 1988. A heat shock operon in Coxiella burnetii produces a major antigen homologous to a protein in both mycobacteria and Escherichia coli. J. Bacteriol. 170:1227-1234.
    • (1988) J. Bacteriol. , vol.170 , pp. 1227-1234
    • Vodkin, M.H.1    Williams, J.C.2
  • 56
    • 0000991152 scopus 로고
    • The structure, function, and genetics of the chaperonin containing TCP-1 (CCT) in eukaryotic cytosol
    • R. I. Morimoto, A. Tissières, and C. Georgopoulos (ed.), Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Willison, K. R., and H. Kubota. 1994. The structure, function, and genetics of the chaperonin containing TCP-1 (CCT) in eukaryotic cytosol, p. 299-312. In R. I. Morimoto, A. Tissières, and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 299-312
    • Willison, K.R.1    Kubota, H.2


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